Combined fractures in the capitellum and the radial head associated with medial capsular avulsion

We present a case with an unusual fracture. A 28-year-old man presented a painful and swollen left elbow after falling down. Radiographs revealed combined fractures in the capitellum and the radial head associated with a medial capsular avulsion. Two osteochondral fragments from the capitellum were found at the operation. One was the free fragment revealed on radiographic examination. Another was not revealed before the operation and was found piercing the fracture line of the radial head. These two fragments were removed. The radial head fracture was reduced and was fixed using two Herbert screws. It is very difficult to detect a fragment of the capitellum that impaled the radial head on a plain radiogram before operation. Also, a capsular injury and/or ligamentous injury is often overlooked. This fact should be kept in mind whenever a non-operatively treated radial head fracture fails to respond as expected.     

Primary Structures of Hemagglutinin-esterase and Spike Glycoproteins of Murine Coronavirus DVIM

Diarrhea virus of infant mice (DVIM) is a member of murine hepatitis viruses (MHVs). The nucleotide sequences of the genes encoding the hemagglutinin-esterase (HE) and the spike (S) glycoproteins from DVIM were determined and compared with those of other MHVs. The deduced amino acid sequence of the HE protein was most similar to that of MHV-S strain (94% identity), and the S protein sequence was most similar to that of MHV-Y strain (90% identity). The DVIM HE protein has a unique N-linked glycosylation site in addition to other glycosylation sites common to many MHV strains. Unlike in some typical MHV strain, such as MHV-A59 and MHV-JHM, the vast majority of the S glycoprotein molecules in DVIM exist an uncleaved form probably due to several amino acid substitutions around the cleavage site. This revised version was published online in July 2006 with corrections to the Cover Date.     

Detection of tmRNA-mediated trans-translation products in Bacillus subtilis

BACKGROUND: Bacterial tmRNA (10Sa RNA) is involved in a trans-translation reaction, which contributes to the degradation of incompletely synthesized peptides and the recycling of stalled ribosomes. To investigate the physiological roles of this reaction in Bacillus subtilis, we devised a system for detecting the proteins that are subject to in vivo trans-translation. RESULTS: The wild-type tmRNA gene (ssrA) in the genome was replaced by a variant ssrA encoding a tag-peptide sequence containing six histidine residues (His-tag) and two aspartic acids at the C-terminus. The His-tagged proteins that accumulated in the cells without degradation were fractionated by Ni2+-NTA column and gel electrophoresis and were detected by Western blotting with an anti-His-tag antibody. The results showed that the trans-translation occurred more frequently at a high temperature (50 degrees C) than at a low temperature (37 degrees C). Two-dimensional (2D) gel electrophoresis of the products revealed many distinct spots, which represent specific target proteins for the trans-translation reaction. Furthermore, the 2D gel patterns of the products from cells cultured at high and low temperatures were apparently different. Several tagged proteins were identified by the N-terminal amino acid sequences of the products. CONCLUSION: Trans-translation occurs more frequently at high temperature than at low temperature, and different proteins are tagged at different temperatures.